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BIO 481 Microbiology > Ch 10 Intro Metabolism > Flashcards

Ch 10 Intro Metabolism Flashcards

(78 cards)

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1
Q

Chemical work

A

Synthesis of complex bio molecules from simpler ones (anabolism)

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2
Q

Transport work

A

Take up nutrients, export waste & maintain ion balances

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3
Q

Mechanical work

A

Cell motility and movement of structures within cell.

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4
Q

Energy

A

Capacity to do work

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5
Q

ATP

A

Adenosine 5’-triphosphate a high E molecule used as cells energy currency

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6
Q

Thermodynamics

A

Study of E changes in a system

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7
Q

1st Law of Thermodynamics

A

E neither created nor destroyed

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8
Q

2nd Law of Thermodynamics

A

Chemical and physical processes proceed such that Entropy increases

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9
Q

Entropy

A

Measure of randomness and/or disorder

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10
Q

Exothermic reactions

A

Give off heat.

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11
Q

Endothermic reactions

A

Absorb heat

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12
Q

Calorie

A

Amt of heat E need to raise 1g water 1 degree C

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13
Q

Joules

A

Units of work capable of being done

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14
Q

Enthalpy

A

Heat content in a system

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15
Q

Free E change

A

Amount of E in a system available to do useful work at constant temp and pressure

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16
Q

Reactions occur spontaneously when

A

The free E of the system decreases

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17
Q

Equilibrium

A

State where no net change is occurring & free E is at a minimum (forward rxn = reverse rxn)

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18
Q

Equilibrium constant ( Keq)

A

[C][D] / [A][B]
( >1 then more products than reactants at equilibrium and will proceed as written

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19
Q

Standard free E change (delta G degree)

A

Free E change for a process at defined conditions of [], pressure, pH, and temp

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20
Q

Delta G degree apostrophe

A

Standard free E change when pH is 7 ( ie most cells)
= -2.303 RT x log Keq
(R=gas constant T=absolute temp)

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21
Q

Gas Constant (R)

A

1.9872 cal/ mol-degree
8.3145 J/mol-degree

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22
Q

Exergonic reaction

A

A rxn than spontaneously goes to completion. Standard free E change is NEGATIVE, Keq > 1

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23
Q

Energy earned

A

Exergonic reactions ( Neg delta G)

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24
Q

Energy spent

A

Endergonic reactions ( used by cells to make ATP to “store” E)

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25
ADP
Adenosine diphosphate
26
Orthophosphate
Pi
27
High phosphate transfer potential
Phosphorylated compound will readily transfer a phosphoryl grp to another molecule (large release of energy occurs)
28
Substrate level phosphorylation
Making ATP using phoshoenolpyruvate (PEP) as source for phosphoryl group
29
Redox reactions
Reactions involving the transfer of electrons from a electron donor to an electron acceptor
30
e- donor
Also called reducing agent or reductant. Donates the e- to the acceptor in a redox rxn
31
e- acceptor
Also called oxidizing agent or oxidant. Accepts e- from the donor in a redox rxn.
32
More e- on a molecule means
More E for that molecule to donate
33
Conjugate redox pair
e- acceptor and e- donor of redox half reaction
34
Equilibrium constant for redox half rxn
Standard reduction potential (E0) ( measure of the tendency of the donor half to lose e-, measured in volts)
35
Redox rxn tower trend
Half Rxn w/ more - E0 pair with half rxn with more + E0 (rxns further apart tend to pair well)
36
NAD+
Nicotinamide adenine dinucleotide
37
Electron transport chain (ETC)
Series of e- carriers that work together to transfer e- from donors to acceptors (like O2) AKA electron transport system. Embedded in a membrane.
38
Molecules involved in ETC
NAD+, NADP+, cytochromes, heme proteins, nonheme proteins, coenzyme Q, flavin adenine dinucleotide (FAD) flavin mononucleotide (FVN)
39
E0 trend in ETC
1st ETC most negative E0, ea slightly less so spontaneous transfer occurs
40
Metabolites
Products of the many reactions carried out by the cell
41
Biochemical pathways
Sets of chemical rxns preformed by organisms that convert starting substrate to one or more products
42
Metabolite flux
Turnover rate of metabolite ( rate it is produced and then used up)
43
Enzymes
Protein catalyst
44
Catalyst
Substance that increases the rate of chemical rxn without being changed permanently
45
How many general classes of enzymes?
6: Oxidireductase, Transferase, Hydrolase, Lyase, Isomerase, Ligase
46
Oxidoreductase
Redox reactions
47
Transferase
Rxns involving transfer of chemical groups between molecules
48
Hydrolase
Hydrolysis
49
Lyase
Breaking of bonds by means other than hydrolysis
50
Isomerase
Rearrange molecules to isomer form
51
Ligase
Joining two molecules using ATP or other nucleoside triphosphate
52
Apoenzyme
Enzyme that requires a cofactor
53
Cofactor
Non protein component required for catalytic activity
54
Holoenzyme
Complete apoenzyme and cofactor complex
55
Cofactor tightly (covalently) linked to apoenzyme
Prosthetic group
56
Loosely attached, able to dissociate cofactor
Coenzyme
57
Activation energy
Energy required to bring substrate molecules together in correct way for reaction to occur. (reach the transition state complex)
58
Active site
Aka catalytic site. Location on enzyme where substrate enzyme complex is formed to catalyze the rxn
59
How do enzymes lower activation energy?
Bind substrates at the active site in the correct orientation for rxn to occur
60
Michaelis constant (Km)
Substrate concentration required for enzyme to reach half maximal velocity (used to quantify the affinity of enzyme for substrate)
61
What does lower Km mean?
Lower substrate concentration at which enzyme catalyzes the rxn (low Km=high affinity for substrate
62
Competitive inhibitor
Molecule that inhibits enzyme function by directly competing with substrate by binding to the active site.
63
Non competitive inhibitors
Inhibit enzyme function by binding to another site on enzyme that alters the shape of the enzyme, rendering it non functional.
64
Ribozyme
Catalytic ribosomes
65
How many ways are metabolic pathways regulated?
3 major ways; metabolic channeling, regulation of gene expression, posttranslational regultation
66
Metabolic channeling
Localizing metabolites and enzymes in different parts of cells
67
Compartmentation
Distribution of enzymes an metabolites among separate cell structures or organelles
68
Regulation of gene expression
Regulates the synthesis of particular enzyme by changing rates of transcription and/or translation to control the amount of enzyme in cell (slow response)
69
Posttranslational regulation
Direct stimulation or inhibition of enzyme activity, two main types: allosteric reg and covalent mod
70
Allosteric Regulation
Allosteric enzymes are altered by non covalent binding of molecule (allosteric effector) at regulatory site separate from active site. Causes a change in enzyme conformation at active site that activates or inhibits enzyme
71
Allosteric effector
Molecule that binds to allosteric enzymes regulatory site to activate or inhibit enzyme function
72
Regulatory site
Site on allosteric enzyme separate from active site that binds a allosteric effector
73
Covalent modification
Activation or inhibition of enzyme via covalent addition or removal of particular functional group (phosphoryl, methyl, or adenylyl)
74
Covalent mod of E.coli glutamine synthetase
Each of 12 subunits can bind adenylic acid———> when all 12 have AMP not active. Removal of AMP allows glutamine formation———> the more removed the more active
75
Allows for more sophisticated and varied stimuli response
Covalent modification systems
76
Pacemaker enzyme
An enzyme that catalyzes the slowest (or rate determining) Rxn in a metabolic pathway
77
Feedback inhibition
Neg feedback mech where end product inhibits the activity of an enzyme in the pathway leading to its formation. Aka end product inhibition
78
Isoenzymes
Different forms of an enzyme that catalyze the same Rxn. Aka isozymes.

BIO 481 Microbiology (12 decks)

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